메뉴 건너뛰기




Volumn 275, Issue 23, 2008, Pages 5865-5872

A novel nucleoside kinase from Burkholderia thailandensis: A member of the phosphofructokinase B-type family of enzymes

Author keywords

Adenosine kinase; Burkholderia thailandensis; Inosine guanosine kinase; Nucleoside kinase; Phosphofructokinase B

Indexed keywords

6 PHOSPHOFRUCTOKINASE ISOENZYME L; ADENOSINE TRIPHOSPHATE; BACTERIAL ENZYME; INOSINE; NUCLEOSIDE KINASE; PURINE NUCLEOSIDE; UNCLASSIFIED DRUG; URIDINE;

EID: 55949092014     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2008.06716.x     Document Type: Article
Times cited : (7)

References (28)
  • 2
    • 33846129777 scopus 로고    scopus 로고
    • The phosphofructokinase-B (MJ0406) from Methanocaldococcus jannaschii represents a nucleoside kinase with a broad substrate specificity
    • Hansen T, Arnfors L, Ladenstein R Schönheit P (2006) The phosphofructokinase-B (MJ0406) from Methanocaldococcus jannaschii represents a nucleoside kinase with a broad substrate specificity. Extremophiles 11, 105 114.
    • (2006) Extremophiles , vol.11 , pp. 105-114
    • Hansen, T.1    Arnfors, L.2    Ladenstein, R.3    Schönheit, P.4
  • 3
    • 0036135847 scopus 로고    scopus 로고
    • Sequence, expression, and characterization of the first archaeal ATP-dependent 6-phosphofructokinase, a non-allosteric enzyme related to the phosphofructokinase-B sugar kinase family, from the hyperthermophilic crenarchaeote Aeropyrum pernix
    • Hansen T Schönheit P (2001) Sequence, expression, and characterization of the first archaeal ATP-dependent 6-phosphofructokinase, a non-allosteric enzyme related to the phosphofructokinase-B sugar kinase family, from the hyperthermophilic crenarchaeote Aeropyrum pernix. Arch Microbiol 177, 62 69.
    • (2001) Arch Microbiol , vol.177 , pp. 62-69
    • Hansen, T.1    Schönheit, P.2
  • 4
    • 0034636799 scopus 로고    scopus 로고
    • Crystal structure of 4-methyl-5-beta-hydroxyethylthiazole kinase from Bacillus subtilis at 1.5 Å resolution
    • Campobasso N, Mathews II, Begley TP Ealick SE (2000) Crystal structure of 4-methyl-5-beta-hydroxyethylthiazole kinase from Bacillus subtilis at 1.5 Å resolution. Biochemistry 39, 7868 7877.
    • (2000) Biochemistry , vol.39 , pp. 7868-7877
    • Campobasso, N.1    Mathews, I.I.2    Begley, T.P.3    Ealick, S.E.4
  • 5
    • 0032868347 scopus 로고    scopus 로고
    • Recombinant expression, purification, and characterization of Toxoplasma gondii adenosine kinase
    • Darling JA, Sullivan WJ Jr., Carter D, Ullman B Roos DS (1999) Recombinant expression, purification, and characterization of Toxoplasma gondii adenosine kinase. Mol Biochem Parasitol 103, 15 23.
    • (1999) Mol Biochem Parasitol , vol.103 , pp. 15-23
    • Darling, J.A.1    Sullivan Jr., W.J.2    Carter, D.3    Ullman, B.4    Roos, D.S.5
  • 6
    • 0032506161 scopus 로고    scopus 로고
    • Structure of human adenosine kinase at 1.5 Å resolution
    • Mathews II, Erion MD Ealick SE (1998) Structure of human adenosine kinase at 1.5 Å resolution. Biochemistry 37, 15607 15620.
    • (1998) Biochemistry , vol.37 , pp. 15607-15620
    • Mathews, I.I.1    Erion, M.D.2    Ealick, S.E.3
  • 7
    • 34848907756 scopus 로고    scopus 로고
    • High resolution crystal structures of Mycobacterium tuberculosis adenosine kinase: Insights into the mechanism and specificity of this novel prokaryotic enzyme
    • Reddy MC, Palaninathan SK, Shetty ND, Owen JL, Watson MD Sacchettini JC (2007) High resolution crystal structures of Mycobacterium tuberculosis adenosine kinase: insights into the mechanism and specificity of this novel prokaryotic enzyme. J Biol Chem 282, 27334 27342.
    • (2007) J Biol Chem , vol.282 , pp. 27334-27342
    • Reddy, M.C.1    Palaninathan, S.K.2    Shetty, N.D.3    Owen, J.L.4    Watson, M.D.5    Sacchettini, J.C.6
  • 8
    • 0032520213 scopus 로고    scopus 로고
    • Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 Å resolution: Insights into a new family of kinase structures
    • Sigrell JA, Cameron AD, Jones TA Mowbray SL (1998) Structure of Escherichia coli ribokinase in complex with ribose and dinucleotide determined to 1.8 Å resolution: insights into a new family of kinase structures. Structure 6, 183 193.
    • (1998) Structure , vol.6 , pp. 183-193
    • Sigrell, J.A.1    Cameron, A.D.2    Jones, T.A.3    Mowbray, S.L.4
  • 10
    • 4644284673 scopus 로고    scopus 로고
    • Crystal structure of an aminoimidazole riboside kinase from Salmonella enterica: Implications for the evolution of the ribokinase superfamily
    • Zhang Y, Dougherty M, Downs DM Ealick SE (2004) Crystal structure of an aminoimidazole riboside kinase from Salmonella enterica: implications for the evolution of the ribokinase superfamily. Structure 12, 1809 1821.
    • (2004) Structure , vol.12 , pp. 1809-1821
    • Zhang, Y.1    Dougherty, M.2    Downs, D.M.3    Ealick, S.E.4
  • 11
    • 29244477827 scopus 로고    scopus 로고
    • Bacterial genome adaptation to niches: Divergence of the potential virulence genes in three Burkholderia species of different survival strategies
    • Kim HS, Schell MA, Yu Y, Ulrich RL, Sarria SH, Nierman WC DeShazer D (2005) Bacterial genome adaptation to niches: divergence of the potential virulence genes in three Burkholderia species of different survival strategies. BMC Genomics 6, 174 187.
    • (2005) BMC Genomics , vol.6 , pp. 174-187
    • Kim, H.S.1    Schell, M.A.2    Yu, Y.3    Ulrich, R.L.4    Sarria, S.H.5    Nierman, W.C.6    Deshazer, D.7
  • 12
    • 0027404023 scopus 로고
    • Convergent evolution of similar enzymatic function on different protein folds: The hexokinase, ribokinase, and galactokinase families of sugar kinases
    • Bork P, Sander C Valencia A (1993) Convergent evolution of similar enzymatic function on different protein folds: the hexokinase, ribokinase, and galactokinase families of sugar kinases. Protein Sci 2, 31 40.
    • (1993) Protein Sci , vol.2 , pp. 31-40
    • Bork, P.1    Sander, C.2    Valencia, A.3
  • 13
    • 0037177252 scopus 로고    scopus 로고
    • Pentavalent ions dependency is a conserved property of adenosine kinase from diverse sources: Identification of a novel motif implicated in phosphate and magnesium ion binding and substrate inhibition
    • Maj MC, Singh B Gupta RS (2002) Pentavalent ions dependency is a conserved property of adenosine kinase from diverse sources: identification of a novel motif implicated in phosphate and magnesium ion binding and substrate inhibition. Biochemistry 41, 4059 4069.
    • (2002) Biochemistry , vol.41 , pp. 4059-4069
    • Maj, M.C.1    Singh, B.2    Gupta, R.S.3
  • 14
    • 0033618324 scopus 로고    scopus 로고
    • Induced fit on sugar binding activates ribokinase
    • Sigrell JA, Cameron AD Mowbray SL (1999) Induced fit on sugar binding activates ribokinase. J Mol Biol 290, 1009 1018.
    • (1999) J Mol Biol , vol.290 , pp. 1009-1018
    • Sigrell, J.A.1    Cameron, A.D.2    Mowbray, S.L.3
  • 15
    • 16844371918 scopus 로고    scopus 로고
    • Characterization of LtsA from Rhodococcus erythropolis, an enzyme with glutamine amidotransferase activity
    • Mitani Y, Meng X, Kamagata Y Tamura T (2005) Characterization of LtsA from Rhodococcus erythropolis, an enzyme with glutamine amidotransferase activity. J Bacteriol 187, 2582 2591.
    • (2005) J Bacteriol , vol.187 , pp. 2582-2591
    • Mitani, Y.1    Meng, X.2    Kamagata, Y.3    Tamura, T.4
  • 16
    • 1842578348 scopus 로고    scopus 로고
    • A novel system for expressing recombinant proteins over a wide temperature range from 4 to 35 degrees C
    • Nakashima N Tamura T (2004) A novel system for expressing recombinant proteins over a wide temperature range from 4 to 35 degrees C. Biotechnol Bioeng 86, 136 148.
    • (2004) Biotechnol Bioeng , vol.86 , pp. 136-148
    • Nakashima, N.1    Tamura, T.2
  • 17
    • 0042071192 scopus 로고    scopus 로고
    • Expression, purification, and characterization of recombinant Saccharomyces cerevisiae adenosine kinase
    • Lu XB, Wu HZ, Ye J, Fan Y Zhang HZ (2003) Expression, purification, and characterization of recombinant Saccharomyces cerevisiae adenosine kinase. Acta Biochim Biophys Sin 35, 666 670.
    • (2003) Acta Biochim Biophys Sin , vol.35 , pp. 666-670
    • Lu, X.B.1    Wu, H.Z.2    Ye, J.3    Fan, Y.4    Zhang, H.Z.5
  • 19
    • 0027076754 scopus 로고
    • Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri
    • Breitung J, Borner G, Scholz S, Linder D, Stetter KO Thauer RK (1992) Salt dependence, kinetic properties and catalytic mechanism of N-formylmethanofuran:tetrahydromethanopterin formyltransferase from the extreme thermophile Methanopyrus kandleri. Eur J Biochem 210, 971 981.
    • (1992) Eur J Biochem , vol.210 , pp. 971-981
    • Breitung, J.1    Borner, G.2    Scholz, S.3    Linder, D.4    Stetter, K.O.5    Thauer, R.K.6
  • 20
    • 33751435355 scopus 로고    scopus 로고
    • Expression of bovine lactoferrin C-lobe in Rhodococcus erythropolis and its purification and characterization
    • Kim WS, Shimazaki K Tamura T (2006) Expression of bovine lactoferrin C-lobe in Rhodococcus erythropolis and its purification and characterization. Biosci Biotechnol Biochem 70, 2641 2645.
    • (2006) Biosci Biotechnol Biochem , vol.70 , pp. 2641-2645
    • Kim, W.S.1    Shimazaki, K.2    Tamura, T.3
  • 21
    • 0242659213 scopus 로고    scopus 로고
    • Identification and characterization of a unique adenosine kinase from Mycobacterium tuberculosis
    • Long MC, Escuyer V Parker WB (2003) Identification and characterization of a unique adenosine kinase from Mycobacterium tuberculosis. J Bacteriol 185, 6548 6555.
    • (2003) J Bacteriol , vol.185 , pp. 6548-6555
    • Long, M.C.1    Escuyer, V.2    Parker, W.B.3
  • 22
    • 0029093265 scopus 로고
    • Cloning of a guanosine-inosine kinase gene of Escherichia coli and characterization of the purified gene product
    • Mori H, Iida A, Teshiba S Fujio T (1995) Cloning of a guanosine-inosine kinase gene of Escherichia coli and characterization of the purified gene product. J Bacteriol 177, 4921 4926.
    • (1995) J Bacteriol , vol.177 , pp. 4921-4926
    • Mori, H.1    Iida, A.2    Teshiba, S.3    Fujio, T.4
  • 24
    • 0034168296 scopus 로고    scopus 로고
    • Development of an improved assay for purine nucleoside kinase activity in cell extracts and detection of inosine kinase activity in Brevibacterium acetylicum ATCC 953, related species, and Corynebacterium flaccumfaciens ATCC 6887
    • Kawasaki H, Usuda Y, Shimaoka M Utagawa T (2000) Development of an improved assay for purine nucleoside kinase activity in cell extracts and detection of inosine kinase activity in Brevibacterium acetylicum ATCC 953, related species, and Corynebacterium flaccumfaciens ATCC 6887. Biosci Biotechnol Biochem 64, 761 766.
    • (2000) Biosci Biotechnol Biochem , vol.64 , pp. 761-766
    • Kawasaki, H.1    Usuda, Y.2    Shimaoka, M.3    Utagawa, T.4
  • 25
    • 0021018456 scopus 로고
    • Purine nucleoside kinases in human T- and B-lymphoblasts
    • Yamada Y, Goto H Ogasawara N (1983) Purine nucleoside kinases in human T- and B-lymphoblasts. Biochim Biophys Acta 761, 34 40.
    • (1983) Biochim Biophys Acta , vol.761 , pp. 34-40
    • Yamada, Y.1    Goto, H.2    Ogasawara, N.3
  • 26
    • 34250899753 scopus 로고    scopus 로고
    • Identification and characterization of human ribokinase and comparison of its properties with E. coli ribokinase and human adenosine kinase
    • Park J, van Koeverden P, Singh B Gupta RS (2007) Identification and characterization of human ribokinase and comparison of its properties with E. coli ribokinase and human adenosine kinase. FEBS Lett 581, 3211 3216.
    • (2007) FEBS Lett , vol.581 , pp. 3211-3216
    • Park, J.1    Van Koeverden, P.2    Singh, B.3    Gupta, R.S.4
  • 27
    • 0034685603 scopus 로고    scopus 로고
    • Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding
    • Schumacher MA, Scott DM, Mathews II, Ealick SE, Roos DS, Ullman B Brennan RG (2000) Crystal structures of Toxoplasma gondii adenosine kinase reveal a novel catalytic mechanism and prodrug binding. J Mol Biol 298, 875 893.
    • (2000) J Mol Biol , vol.298 , pp. 875-893
    • Schumacher, M.A.1    Scott, D.M.2    Mathews, I.I.3    Ealick, S.E.4    Roos, D.S.5    Ullman, B.6    Brennan, R.G.7
  • 28
    • 55949088666 scopus 로고    scopus 로고
    • A novel enzymatic method for measuring mizoribine phosphate levels in serum
    • in press.
    • Ota H, Yasuda Y, Sakasegawa S, Imamura S Tamura T (2008) A novel enzymatic method for measuring mizoribine phosphate levels in serum. J Biosci Bioeng 5, in press.
    • (2008) J Biosci Bioeng , vol.5
    • Ota, H.1    Yasuda, Y.2    Sakasegawa, S.3    Imamura, S.4    Tamura, T.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.